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compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Focusing on the mechanism linking complex I and ATP synthase depicted in figure 3 in the article, compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

 

 

matrix side or n side NADH+H+ NAD+ complex I UU booobe putative proton current by Brownian motion ADP + Pi a subunit F1 ATP synthase OH HO ОН ОН ОН ОН FO ATP synthase HO OH putative proton tunnelling through a subunit ATP ОН ОН ОН ОН ОН U U o o o o o o o o o o o glutamic 58 of c subunit periplsmatic side or p side Figure 3. A possible H+ circuit inside respiring membrane. The phosphate groups of phospholipids on both sides of the membrane are shown by brown ellipsoids. The image proposes that the H+ (red dotted line) are transferred to the Glu 58 (E58) at the centre of subunit c through subunit a of ATP synthase by proton tunnelling. H+ would flow from the periplasmic side, always bound to phospholipid heads. This can be arranged in each layer of the membrane.
Transcribed Image Text:matrix side or n side NADH+H+ NAD+ complex I UU booobe putative proton current by Brownian motion ADP + Pi a subunit F1 ATP synthase OH HO ОН ОН ОН ОН FO ATP synthase HO OH putative proton tunnelling through a subunit ATP ОН ОН ОН ОН ОН U U o o o o o o o o o o o glutamic 58 of c subunit periplsmatic side or p side Figure 3. A possible H+ circuit inside respiring membrane. The phosphate groups of phospholipids on both sides of the membrane are shown by brown ellipsoids. The image proposes that the H+ (red dotted line) are transferred to the Glu 58 (E58) at the centre of subunit c through subunit a of ATP synthase by proton tunnelling. H+ would flow from the periplasmic side, always bound to phospholipid heads. This can be arranged in each layer of the membrane.
matrix side or N side H+ NADH + H+ H+ NAD+1 H+ complex I H+ H+ H+ H+ Redox coupling (first coupling) H+ H+ H+ H+ FADH2 complex II 410 0 0 0 0 Wet CooWett ooooooo H+ H+ H+ FAD H+ H+ H+ H+ complex III H+ H+ ! H+ H*H* H+ non Cit C H+ H+ H+ 1/2 O₂ + 2H+ + 2 e¯ | H₂O DO H+ H+ H+ H+ complex IV H+ H+ H+ H+ proton coupling (second coupling) H+ ADP + P₁ H+ DOOOOG H+ F1 ATP synthase H+ H+ H+ FO ATP synthase H+ H+ H+ H+ H+ ATP periplasmatic side or p side Figure 1. Schematic of the 1961 Mitchell chemiosmotic theory. A delocalized coupling is depicted among protons extruded by the electron transport chain (ETC) and ATP synthesis. The overall process is arbitrarily divided in the two phases: the 'RedOx coupling', in which the proton movement is operated by the ETC, and the 'proton coupling', in which proton movement is coupled with ATP synthesis, by F,F₁-ATP synthase.
Transcribed Image Text:matrix side or N side H+ NADH + H+ H+ NAD+1 H+ complex I H+ H+ H+ H+ Redox coupling (first coupling) H+ H+ H+ H+ FADH2 complex II 410 0 0 0 0 Wet CooWett ooooooo H+ H+ H+ FAD H+ H+ H+ H+ complex III H+ H+ ! H+ H*H* H+ non Cit C H+ H+ H+ 1/2 O₂ + 2H+ + 2 e¯ | H₂O DO H+ H+ H+ H+ complex IV H+ H+ H+ H+ proton coupling (second coupling) H+ ADP + P₁ H+ DOOOOG H+ F1 ATP synthase H+ H+ H+ FO ATP synthase H+ H+ H+ H+ H+ ATP periplasmatic side or p side Figure 1. Schematic of the 1961 Mitchell chemiosmotic theory. A delocalized coupling is depicted among protons extruded by the electron transport chain (ETC) and ATP synthesis. The overall process is arbitrarily divided in the two phases: the 'RedOx coupling', in which the proton movement is operated by the ETC, and the 'proton coupling', in which proton movement is coupled with ATP synthesis, by F,F₁-ATP synthase.
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